Regulating mitochondrial outer membrane proteins by ubiquitination and proteasomal degradation.
Regulating mitochondrial outer membrane proteins by ubiquitination and proteasomal degradation.
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DOI:
10.1016/j.ceb.2011.05.007
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发表时间:
2011-08
影响因子:
7.5
通讯作者:
Youle, Richard J.
中科院分区:
文献类型:
--
作者:
Karbowski, Mariusz;Youle, Richard J.
Mitochondrial outer membrane proteins have been found to be ubiquitinated and degraded by the proteasome. This process shares at least one component of the ERAD pathway of ER membrane protein degradation, the AAA ATPase cdc48/p97/VCP, thought to extract integral membrane proteins from the lipid bilayer and chaperone them to the proteasome. Proteasomal degradation of the outer mitochondrial membrane protein Mcl-1 regulates apoptosis whereas Parkin-mediated ubiquitination and degradation of Mitofusins can inhibit mitochondrial fusion and promote mitophagy. The breadth of outer mitochondrial membrane ubiquitin/proteasome substrates and the physiological relevance of their turnover is only beginning to be understood.
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